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AB10B_ARATH
ID   AB10B_ARATH             Reviewed;        1227 AA.
AC   Q9SGY1;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 2.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=ABC transporter B family member 10;
DE            Short=ABC transporter ABCB.10;
DE            Short=AtABCB10;
DE   AltName: Full=Multidrug resistance protein 10;
DE   AltName: Full=P-glycoprotein 10;
GN   Name=ABCB10; Synonyms=MDR10, PGP10; OrderedLocusNames=At1g10680;
GN   ORFNames=F20B24.12;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   PROTEIN SEQUENCE OF 22-28; 29-40; 953-958 AND 1247-1254, AND INTERACTION
RP   WITH NPA.
RX   PubMed=16243904; DOI=10.1105/tpc.105.035816;
RA   Terasaka K., Blakeslee J.J., Titapiwatanakun B., Peer W.A.,
RA   Bandyopadhyay A., Makam S.N., Lee O.R., Richards E.L., Murphy A.S.,
RA   Sato F., Yazaki K.;
RT   "PGP4, an ATP binding cassette P-glycoprotein, catalyzes auxin transport in
RT   Arabidopsis thaliana roots.";
RL   Plant Cell 17:2922-2939(2005).
RN   [4]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=11346655; DOI=10.1074/jbc.m103104200;
RA   Sanchez-Fernandez R., Davies T.G., Coleman J.O., Rea P.A.;
RT   "The Arabidopsis thaliana ABC protein superfamily, a complete inventory.";
RL   J. Biol. Chem. 276:30231-30244(2001).
RN   [5]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=18299247; DOI=10.1016/j.tplants.2008.02.001;
RA   Verrier P.J., Bird D., Burla B., Dassa E., Forestier C., Geisler M.,
RA   Klein M., Kolukisaoglu H.U., Lee Y., Martinoia E., Murphy A., Rea P.A.,
RA   Samuels L., Schulz B., Spalding E.J., Yazaki K., Theodoulou F.L.;
RT   "Plant ABC proteins - a unified nomenclature and updated inventory.";
RL   Trends Plant Sci. 13:151-159(2008).
RN   [6]
RP   INDUCTION BY NAC045 AND NAC086, AND TISSUE SPECIFICITY.
RX   PubMed=25081480; DOI=10.1126/science.1253736;
RA   Furuta K.M., Yadav S.R., Lehesranta S., Belevich I., Miyashima S.,
RA   Heo J.O., Vaten A., Lindgren O., De Rybel B., Van Isterdael G.,
RA   Somervuo P., Lichtenberger R., Rocha R., Thitamadee S., Taehtiharju S.,
RA   Auvinen P., Beeckman T., Jokitalo E., Helariutta Y.;
RT   "Plant development. Arabidopsis NAC45/86 direct sieve element morphogenesis
RT   culminating in enucleation.";
RL   Science 345:933-937(2014).
CC   -!- SUBUNIT: Interacts with 1-naphthylphthalamic acid (NPA).
CC       {ECO:0000269|PubMed:16243904}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255|PROSITE-ProRule:PRU00441};
CC       Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC   -!- TISSUE SPECIFICITY: Expressed in the sieve elements.
CC       {ECO:0000269|PubMed:25081480}.
CC   -!- INDUCTION: Regulated by the transcription factors NAC045 and NAC086.
CC       {ECO:0000269|PubMed:25081480}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC       Multidrug resistance exporter (TC 3.A.1.201) subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF17668.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC009398; AAF17668.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE28628.1; -; Genomic_DNA.
DR   PIR; B86240; B86240.
DR   RefSeq; NP_172538.1; NM_100944.2.
DR   AlphaFoldDB; Q9SGY1; -.
DR   SMR; Q9SGY1; -.
DR   STRING; 3702.AT1G10680.1; -.
DR   PaxDb; Q9SGY1; -.
DR   PRIDE; Q9SGY1; -.
DR   ProteomicsDB; 245080; -.
DR   EnsemblPlants; AT1G10680.1; AT1G10680.1; AT1G10680.
DR   GeneID; 837611; -.
DR   Gramene; AT1G10680.1; AT1G10680.1; AT1G10680.
DR   KEGG; ath:AT1G10680; -.
DR   Araport; AT1G10680; -.
DR   TAIR; locus:2019958; AT1G10680.
DR   eggNOG; KOG0055; Eukaryota.
DR   HOGENOM; CLU_000604_17_2_1; -.
DR   InParanoid; Q9SGY1; -.
DR   OMA; YRVRHEV; -.
DR   OrthoDB; 186078at2759; -.
DR   PhylomeDB; Q9SGY1; -.
DR   BioCyc; ARA:AT1G10680-MON; -.
DR   PRO; PR:Q9SGY1; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9SGY1; baseline and differential.
DR   Genevisible; Q9SGY1; AT.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR   GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR   Gene3D; 1.20.1560.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR011527; ABC1_TM_dom.
DR   InterPro; IPR036640; ABC1_TM_sf.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR039421; Type_1_exporter.
DR   PANTHER; PTHR24221; PTHR24221; 1.
DR   Pfam; PF00664; ABC_membrane; 2.
DR   Pfam; PF00005; ABC_tran; 2.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF90123; SSF90123; 2.
DR   PROSITE; PS50929; ABC_TM1F; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   1: Evidence at protein level;
KW   ATP-binding; Direct protein sequencing; Glycoprotein; Membrane;
KW   Nucleotide-binding; Reference proteome; Repeat; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..1227
FT                   /note="ABC transporter B family member 10"
FT                   /id="PRO_0000227921"
FT   TRANSMEM        38..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        90..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        169..188
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        194..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        269..289
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        297..317
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        663..683
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        704..724
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        784..804
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        806..826
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        889..909
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        927..947
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          41..330
FT                   /note="ABC transmembrane type-1 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          361..597
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          662..949
FT                   /note="ABC transmembrane type-1 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          982..1218
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         396..403
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         1017..1024
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   CARBOHYD        758
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        834
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1227 AA;  134475 MW;  4B1AB2A1DF082348 CRC64;
     MQPSNDPAIV DMAAAEKEKK RPSVSFLKLF SFADFYDCVL MALGSIGACI HGASVPVFFI
     FFGKLINIIG LAYLFPQEAS HKVAKYSLDF VYLSVVILFS SWLEVACWMH TGERQAAKIR
     KAYLRSMLSQ DISLFDTEIS TGEVISAITS EILVVQDAIS EKVGNFMHFI SRFIAGFAIG
     FASVWQISLV TLSIVPFIAL AGGIYAFVSS GLIVRVRKSY VKANEIAEEV IGNVRTVQAF
     TGEEKAVSSY QGALRNTYNY GRKAGLAKGL GLGSLHFVLF LSWALLIWFT SIVVHKGIAN
     GGESFTTMLN VVIAGLSLGQ AAPDISTFMR ASAAAYPIFQ MIERNTEDKT GRKLGNVNGD
     ILFKDVTFTY PSRPDVVIFD KLNFVIPAGK VVALVGGSGS GKSTMISLIE RFYEPTDGAV
     MLDGNDIRYL DLKWLRGHIG LVNQEPVLFA TTIRENIMYG KDDATSEEIT NAAKLSEAIS
     FINNLPEGFE TQVGERGIQL SGGQKQRISI SRAIVKNPSI LLLDEATSAL DAESEKIVQE
     ALDRVMVGRT TVVVAHRLST VRNADIIAVV GGGKIIESGS HDELISNPDG AYSSLLRIQE
     AASPNLNHTP SLPVSTKPLP ELPITETTSS IHQSVNQPDT TKQAKVTVGR LYSMIRPDWK
     YGLCGTLGSF IAGSQMPLFA LGIAQALVSY YMDWETTQNE VKRISILFCC GSVITVIVHT
     IEHTTFGIMG ERLTLRVRQK MFSAILRNEI GWFDKVDNTS SMLASRLESD ATLLRTIVVD
     RSTILLENLG LVVTAFIISF ILNWRLTLVV LATYPLIISG HISEKIFMQG YGGNLSKAYL
     KANMLAGESI SNIRTVVAFC AEEKVLDLYS KELLEPSERS FRRGQMAGIL YGVSQFFIFS
     SYGLALWYGS ILMEKGLSSF ESVMKTFMVL IVTALVMGEV LALAPDLLKG NQMVVSVFEL
     LDRRTQVVGD TGEELSNVEG TIELKGVHFS YPSRPDVTIF SDFNLLVPSG KSMALVGQSG
     SGKSSVLSLV LRFYDPTAGI IMIDGQDIKK LKLKSLRRHI GLVQQEPALF ATTIYENILY
     GKEGASESEV MEAAKLANAH SFISSLPEGY STKVGERGIQ MSGGQRQRIA IARAVLKNPE
     ILLLDEATSA LDVESERVVQ QALDRLMRDR TTVVVAHRLS TIKNSDMISV IQDGKIIEQG
     SHNILVENKN GPYSKLISLQ QRQRHHP
 
 
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